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Myocyte-specific enhancer factor 2C

 MEF2C_MOUSE             Reviewed;         474 AA.
Q8CFN5; Q8R0H1; Q9D7L0; Q9QW20;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 2.
30-AUG-2017, entry version 144.
RecName: Full=Myocyte-specific enhancer factor 2C;
Name=Mef2c;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=8506376; DOI=10.1073/pnas.90.11.5282;
Martin J.F., Schwarz J.J., Olson E.N.;
"Myocyte enhancer factor (MEF) 2C: a tissue-restricted member of the
MEF-2 family of transcription factors.";
Proc. Natl. Acad. Sci. U.S.A. 90:5282-5286(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=C57BL/6J; TISSUE=Tongue;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY.
PubMed=9013788; DOI=10.1016/S0169-328X(96)00135-0;
Lin X., Shah S., Bulleit R.F.;
"The expression of MEF2 genes is implicated in CNS neuronal
differentiation.";
Brain Res. Mol. Brain Res. 42:307-316(1996).
[5]
PHOSPHORYLATION AT SER-59, AND MUTAGENESIS OF SER-59.
PubMed=8663403; DOI=10.1074/jbc.271.29.17199;
Molkentin J.D., Li L., Olson E.N.;
"Phosphorylation of the MADS-Box transcription factor MEF2C enhances
its DNA binding activity.";
J. Biol. Chem. 271:17199-17204(1996).
[6]
FUNCTION.
PubMed=9162005; DOI=10.1126/science.276.5317.1404;
Lin Q., Schwarz J., Bucana C., Olson E.N.;
"Control of mouse cardiac morphogenesis and myogenesis by
transcription factor MEF2C.";
Science 276:1404-1407(1997).
[7]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=9778514;
Lin Q., Lu J., Yanagisawa H., Webb R., Lyons G.E., Richardson J.A.,
Olson E.N.;
"Requirement of the MADS-box transcription factor MEF2C for vascular
development.";
Development 125:4565-4574(1998).
[8]
INTERACTION WITH HDAC7.
PubMed=11279209; DOI=10.1074/jbc.M101508200;
Dressel U., Bailey P.J., Wang S.-C.M., Downes M., Evans R.M.,
Muscat G.E.O.;
"A dynamic role for HDAC7 in MEF2-mediated muscle differentiation.";
J. Biol. Chem. 276:17007-17013(2001).
[9]
INTERACTION WITH CARM1.
PubMed=11713257; DOI=10.1074/jbc.M109835200;
Chen S.L., Loffler K.A., Chen D., Stallcup M.R., Muscat G.E.;
"The coactivator-associated arginine methyltransferase is necessary
for muscle differentiation: CARM1 coactivates myocyte enhancer factor-
2.";
J. Biol. Chem. 277:4324-4333(2002).
[10]
TISSUE SPECIFICITY OF ISOFORMS.
PubMed=15340086; DOI=10.1128/MCB.24.18.8264-8275.2004;
Zhu B., Gulick T.;
"Phosphorylation and alternative pre-mRNA splicing converge to
regulate myocyte enhancer factor 2C activity.";
Mol. Cell. Biol. 24:8264-8275(2004).
[11]
TISSUE SPECIFICITY OF ISOFORMS.
PubMed=15834131; DOI=10.1074/jbc.M502491200;
Zhu B., Ramachandran B., Gulick T.;
"Alternative pre-mRNA splicing governs expression of a conserved
acidic transactivation domain in myocyte enhancer factor 2 factors of
striated muscle and brain.";
J. Biol. Chem. 280:28749-28760(2005).
[12]
INTERACTION WITH MYOCD.
PubMed=16818234; DOI=10.1016/j.molcel.2006.05.026;
Creemers E.E., Sutherland L.B., Oh J., Barbosa A.C., Olson E.N.;
"Coactivation of MEF2 by the SAP domain proteins myocardin and
MASTR.";
Mol. Cell 23:83-96(2006).
[13]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=18438409; DOI=10.1038/ni.1609;
Wilker P.R., Kohyama M., Sandau M.M., Albring J.C., Nakagawa O.,
Schwarz J.J., Murphy K.M.;
"Transcription factor Mef2c is required for B cell proliferation and
survival after antigen receptor stimulation.";
Nat. Immunol. 9:603-612(2008).
[14]
ACETYLATION AT LYS-4, DNA-BINDING, IDENTIFICATION BY MASS
SPECTROMETRY, FUNCTION, AND MUTAGENESIS OF ARG-3 AND LYS-4.
PubMed=18086704; DOI=10.1093/nar/gkm1114;
Angelelli C., Magli A., Ferrari D., Ganassi M., Matafora V.,
Parise F., Razzini G., Bachi A., Ferrari S., Molinari S.;
"Differentiation-dependent lysine 4 acetylation enhances MEF2C binding
to DNA in skeletal muscle cells.";
Nucleic Acids Res. 36:915-928(2008).
[15]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=18599438; DOI=10.1073/pnas.0802679105;
Barbosa A.C., Kim M.S., Ertunc M., Adachi M., Nelson E.D.,
McAnally J., Richardson J.A., Kavalali E.T., Monteggia L.M.,
Bassel-Duby R., Olson E.N.;
"MEF2C, a transcription factor that facilitates learning and memory by
negative regulation of synapse numbers and function.";
Proc. Natl. Acad. Sci. U.S.A. 105:9391-9396(2008).
[16]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18599437; DOI=10.1073/pnas.0802876105;
Li H., Radford J.C., Ragusa M.J., Shea K.L., McKercher S.R.,
Zaremba J.D., Soussou W., Nie Z., Kang Y.J., Nakanishi N., Okamoto S.,
Roberts A.J., Schwarz J.J., Lipton S.A.;
"Transcription factor MEF2C influences neural stem/progenitor cell
differentiation and maturation in vivo.";
Proc. Natl. Acad. Sci. U.S.A. 105:9397-9402(2008).
[17]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19211936; DOI=10.1182/blood-2008-07-167577;
Gekas C., Rhodes K.E., Gereige L.M., Helgadottir H., Ferrari R.,
Kurdistani S.K., Montecino-Rodriguez E., Bassel-Duby R., Olson E.,
Krivtsov A.V., Armstrong S., Orkin S.H., Pellegrini M., Mikkola H.K.;
"Mef2C is a lineage-restricted target of Scl/Tal1 and regulates
megakaryopoiesis and B-cell homeostasis.";
Blood 113:3461-3471(2009).
[18]
INTERACTION WITH LIPN1.
PubMed=19753306; DOI=10.1371/journal.pone.0007031;
Liu G.H., Gerace L.;
"Sumoylation regulates nuclear localization of lipin-1alpha in
neuronal cells.";
PLoS ONE 4:E7031-E7031(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-106; SER-110;
SER-222 AND SER-240, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108
(ISOFORMS 4 AND 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[20]
INTERACTION WITH AKAP13.
PubMed=20139090; DOI=10.1074/jbc.M110.106856;
Mayers C.M., Wadell J., McLean K., Venere M., Malik M., Shibata T.,
Driggers P.H., Kino T., Guo X.C., Koide H., Gorivodsky M.,
Grinberg A., Mukhopadhyay M., Abu-Asab M., Westphal H., Segars J.H.;
"The Rho guanine nucleotide exchange factor AKAP13 (BRX) is essential
for cardiac development in mice.";
J. Biol. Chem. 285:12344-12354(2010).
[21]
INTERACTION WITH FOXK1.
PubMed=22956541; DOI=10.1242/jcs.105239;
Shi X., Wallis A.M., Gerard R.D., Voelker K.A., Grange R.W.,
DePinho R.A., Garry M.G., Garry D.J.;
"Foxk1 promotes cell proliferation and represses myogenic
differentiation by regulating Foxo4 and Mef2.";
J. Cell Sci. 125:5329-5337(2012).
-!- FUNCTION: Transcription activator which binds specifically to the
MEF2 element present in the regulatory regions of many muscle-
specific genes. Controls cardiac morphogenesis and myogenesis, and
is also involved in vascular development. May also be involved in
neurogenesis and in the development of cortical architecture.
Isoform 3 and isoform 4, which lack the repressor domain, are more
active than isoform 1, isoform 2 and isoform 5 (By similarity).
Plays an essential role in hippocampal-dependent learning and
memory by suppressing the number of excitatory synapses and thus
regulating basal and evoked synaptic transmission. Crucial for
normal neuronal development, distribution, and electrical activity
in the neocortex. Necessary for proper development of
megakaryocytes and platelets and for bone marrow B-lymphopoiesis.
Required for B-cell survival and proliferation in response to BCR
stimulation, efficient IgG1 antibody responses to T-cell-dependent
antigens and for normal induction of germinal center B-cells.
{ECO:0000250|UniProtKB:Q06413, ECO:0000269|PubMed:18086704,
ECO:0000269|PubMed:18438409, ECO:0000269|PubMed:18599437,
ECO:0000269|PubMed:18599438, ECO:0000269|PubMed:19211936,
ECO:0000269|PubMed:9162005, ECO:0000269|PubMed:9778514}.
-!- SUBUNIT: Forms a complex with class II HDACs in undifferentiating
cells. On myogenic differentiation, HDACs are released into the
cytoplasm allowing MEF2s to interact with other proteins for
activation. Interacts with EP300 in differentiating cells; the
interaction acetylates MEF2C leading to increased DNA binding and
activation (By similarity). Interacts with HDAC7 and CARM1
(PubMed:11279209, PubMed:11713257). Interacts with HDAC4, HDAC7
AND HDAC9; the interaction with HDACs represses transcriptional
activity (By similarity). Interacts with LPIN1 (PubMed:19753306).
Interacts with MYOCD (PubMed:16818234). Interacts with AKAP13
(PubMed:20139090). Interacts with FOXK1; the interaction inhibits
MEF2C transactivation activity (PubMed:22956541).
{ECO:0000250|UniProtKB:Q06413, ECO:0000269|PubMed:11279209,
ECO:0000269|PubMed:11713257, ECO:0000269|PubMed:16818234,
ECO:0000269|PubMed:19753306, ECO:0000269|PubMed:20139090,
ECO:0000269|PubMed:22956541}.
-!- INTERACTION:
Q91V92:Acly; NbExp=3; IntAct=EBI-643822, EBI-644049;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00251}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q8CFN5-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q8CFN5-2; Sequence=VSP_012504;
Name=3;
IsoId=Q8CFN5-3; Sequence=VSP_012505;
Name=4;
IsoId=Q8CFN5-4; Sequence=VSP_012501, VSP_012502, VSP_012503,
VSP_012504, VSP_012505;
Note=Contains a phosphothreonine at position 108.
{ECO:0000244|PubMed:21183079};
Name=5;
IsoId=Q8CFN5-5; Sequence=VSP_012501, VSP_012502, VSP_012503;
Note=Contains a phosphothreonine at position 108.
{ECO:0000244|PubMed:21183079};
-!- TISSUE SPECIFICITY: Widely expressed though mainly restricted to
skeletal and cardiac muscle, brain, neurons and lymphocytes. Beta
beta domain-lacking isoforms are the most predominantly expressed
in all tissues including skeletal and cardiac muscle and brain.
Only brain expresses all isoforms. Expression occurs primarily in
the internal granule cell layer of the olfactory bulb, cortex,
thalamus, hippocampus and cerebellum. Low levels in the cerebellum
and hindbrain. Expressed throughout the cortex, including the
frontal and entorhinal cortex, dentate gyrus, and basolateral
amygdala. Selectively expressed in B-cells but not in T-cells, and
its expression increases as B-cells mature.
{ECO:0000269|PubMed:15340086, ECO:0000269|PubMed:15834131,
ECO:0000269|PubMed:18438409, ECO:0000269|PubMed:18599438,
ECO:0000269|PubMed:8506376, ECO:0000269|PubMed:9013788}.
-!- DEVELOPMENTAL STAGE: Expressed in developing endothelial cells and
smooth muscle cells, as well as in surrounding mesenchyme, during
embryogenesis. Up-regulated during myogenesis.
{ECO:0000269|PubMed:9778514}.
-!- DOMAIN: The beta domain, missing in a number of isoforms, is
required for enhancement of transcriptional activity.
{ECO:0000250}.
-!- PTM: Phosphorylation on Ser-59 enhances DNA binding activity (By
similarity). Phosphorylation on Ser-396 is required for Lys-391
sumoylation and inhibits transcriptional activity. {ECO:0000250,
ECO:0000269|PubMed:8663403}.
-!- PTM: Acetylated by p300 on several sites in diffentiating myocytes
(By similarity). Acetylation on Lys-4 increases DNA binding and
transactivation. {ECO:0000250, ECO:0000269|PubMed:18086704}.
-!- PTM: Sumoylated on Lys-391 with SUMO2 but not by SUMO1 represses
transcriptional activity. {ECO:0000250}.
-!- PTM: Proteolytically cleaved in cerebellar granule neurons,
probably by caspase 7, following neurotoxicity. Preferentially
cleaves the CDK5-mediated hyperphosphorylated form which leads to
neuron apoptosis and transcriptional inactivation (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice show impairment in hippocampal-
dependent learning and also increase in the number of excitatory
synapses and potentiation of basal and evoked synaptic
transmission. Mice surviving to adulthood manifest smaller,
apparently less mature neurons and smaller whole brain size, with
resultant aberrant electrophysiology and behavior. Mice exhibit
thrombocytopenia and a defect in B-lymphopoiesis.
{ECO:0000269|PubMed:18599437, ECO:0000269|PubMed:18599438,
ECO:0000269|PubMed:19211936}.
-!- SIMILARITY: Belongs to the MEF2 family. {ECO:0000305}.
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EMBL; AK009139; BAB26099.1; -; mRNA.
EMBL; BC026841; AAH26841.1; -; mRNA.
EMBL; BC037731; AAH37731.1; -; mRNA.
EMBL; BC057650; AAH57650.1; -; mRNA.
CCDS; CCDS26664.1; -. [Q8CFN5-4]
CCDS; CCDS49320.1; -. [Q8CFN5-2]
CCDS; CCDS84042.1; -. [Q8CFN5-1]
CCDS; CCDS84043.1; -. [Q8CFN5-3]
CCDS; CCDS84045.1; -. [Q8CFN5-5]
RefSeq; NP_001334493.1; NM_001347564.1. [Q8CFN5-1]
RefSeq; NP_001334495.1; NM_001347566.1. [Q8CFN5-1]
RefSeq; NP_001334496.1; NM_001347567.1. [Q8CFN5-1]
RefSeq; NP_001334497.1; NM_001347568.1. [Q8CFN5-5]
RefSeq; NP_001334498.1; NM_001347569.1. [Q8CFN5-5]
RefSeq; NP_001334500.1; NM_001347571.1. [Q8CFN5-3]
RefSeq; NP_001334501.1; NM_001347572.1. [Q8CFN5-3]
RefSeq; NP_001334502.1; NM_001347573.1. [Q8CFN5-3]
RefSeq; NP_001334503.1; NM_001347574.1. [Q8CFN5-3]
RefSeq; NP_001334504.1; NM_001347575.1. [Q8CFN5-3]
RefSeq; NP_001334505.1; NM_001347576.1. [Q8CFN5-3]
RefSeq; NP_001334506.1; NM_001347577.1. [Q8CFN5-3]
RefSeq; NP_079558.1; NM_025282.3. [Q8CFN5-4]
RefSeq; XP_006517186.1; XM_006517123.2. [Q8CFN5-1]
RefSeq; XP_006517187.1; XM_006517124.3. [Q8CFN5-1]
RefSeq; XP_006517189.1; XM_006517126.2. [Q8CFN5-5]
RefSeq; XP_006517195.1; XM_006517132.3. [Q8CFN5-4]
RefSeq; XP_011242794.1; XM_011244492.2. [Q8CFN5-1]
RefSeq; XP_017170894.1; XM_017315405.1. [Q8CFN5-1]
UniGene; Mm.24001; -.
UniGene; Mm.451574; -.
UniGene; Mm.487610; -.
PDB; 5F28; X-ray; 2.90 A; A/B/C/D=1-95.
PDBsum; 5F28; -.
ProteinModelPortal; Q8CFN5; -.
SMR; Q8CFN5; -.
BioGrid; 201383; 12.
DIP; DIP-49524N; -.
ELM; Q8CFN5; -.
IntAct; Q8CFN5; 6.
MINT; MINT-1551742; -.
STRING; 10090.ENSMUSP00000132547; -.
iPTMnet; Q8CFN5; -.
PhosphoSitePlus; Q8CFN5; -.
PaxDb; Q8CFN5; -.
PeptideAtlas; Q8CFN5; -.
PRIDE; Q8CFN5; -.
Ensembl; ENSMUST00000185052; ENSMUSP00000138826; ENSMUSG00000005583. [Q8CFN5-5]
Ensembl; ENSMUST00000197146; ENSMUSP00000143227; ENSMUSG00000005583. [Q8CFN5-3]
Ensembl; ENSMUST00000197681; ENSMUSP00000143420; ENSMUSG00000005583. [Q8CFN5-3]
Ensembl; ENSMUST00000198199; ENSMUSP00000143742; ENSMUSG00000005583. [Q8CFN5-4]
Ensembl; ENSMUST00000199019; ENSMUSP00000143401; ENSMUSG00000005583. [Q8CFN5-1]
Ensembl; ENSMUST00000199105; ENSMUSP00000143212; ENSMUSG00000005583. [Q8CFN5-1]
Ensembl; ENSMUST00000199450; ENSMUSP00000143315; ENSMUSG00000005583. [Q8CFN5-2]
GeneID; 17260; -.
KEGG; mmu:17260; -.
UCSC; uc007rie.2; mouse. [Q8CFN5-4]
UCSC; uc007rih.2; mouse. [Q8CFN5-5]
UCSC; uc007rii.3; mouse. [Q8CFN5-3]
CTD; 4208; -.
MGI; MGI:99458; Mef2c.
eggNOG; KOG0014; Eukaryota.
eggNOG; COG5068; LUCA.
GeneTree; ENSGT00390000011828; -.
HOGENOM; HOG000230620; -.
HOVERGEN; HBG053944; -.
InParanoid; Q8CFN5; -.
KO; K04454; -.
PhylomeDB; Q8CFN5; -.
TreeFam; TF314067; -.
Reactome; R-MMU-375170; CDO in myogenesis.
PRO; PR:Q8CFN5; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000005583; -.
CleanEx; MM_MEF2C; -.
ExpressionAtlas; Q8CFN5; baseline and differential.
Genevisible; Q8CFN5; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:Alzheimers_University_of_Toronto.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
GO; GO:0003680; F:AT DNA binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; IDA:MGI.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
GO; GO:0071837; F:HMG box domain binding; IPI:UniProtKB.
GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0000983; F:transcription factor activity, RNA polymerase II core promoter sequence-specific; ISS:UniProtKB.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:NTNU_SB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0001782; P:B cell homeostasis; IMP:UniProtKB.
GO; GO:0042100; P:B cell proliferation; IMP:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
GO; GO:0001568; P:blood vessel development; IMP:MGI.
GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
GO; GO:0055007; P:cardiac muscle cell differentiation; IGI:MGI.
GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IMP:MGI.
GO; GO:0003211; P:cardiac ventricle formation; IMP:UniProtKB.
GO; GO:0060536; P:cartilage morphogenesis; IMP:MGI.
GO; GO:0045165; P:cell fate commitment; IMP:MGI.
GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:Alzheimers_University_of_Toronto.
GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
GO; GO:0035690; P:cellular response to drug; IDA:UniProtKB.
GO; GO:0071498; P:cellular response to fluid shear stress; IDA:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; ISS:UniProtKB.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISS:UniProtKB.
GO; GO:0035984; P:cellular response to trichostatin A; IDA:UniProtKB.
GO; GO:0002062; P:chondrocyte differentiation; IGI:MGI.
GO; GO:0021542; P:dentate gyrus development; IEA:Ensembl.
GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:MGI.
GO; GO:0001958; P:endochondral ossification; IMP:MGI.
GO; GO:2001013; P:epithelial cell proliferation involved in renal tubule morphogenesis; IMP:UniProtKB.
GO; GO:0060079; P:excitatory postsynaptic potential; IMP:Alzheimers_University_of_Toronto.
GO; GO:0002467; P:germinal center formation; IMP:UniProtKB.
GO; GO:0072102; P:glomerulus morphogenesis; IMP:UniProtKB.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0001947; P:heart looping; IMP:UniProtKB.
GO; GO:0006959; P:humoral immune response; IMP:UniProtKB.
GO; GO:0007611; P:learning or memory; IMP:UniProtKB.
GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
GO; GO:0030318; P:melanocyte differentiation; IMP:UniProtKB.
GO; GO:0030224; P:monocyte differentiation; IMP:MGI.
GO; GO:0007521; P:muscle cell fate determination; IMP:MGI.
GO; GO:0014902; P:myotube differentiation; IEA:Ensembl.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:UniProtKB.
GO; GO:0030279; P:negative regulation of ossification; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0072160; P:nephron tubule epithelial cell differentiation; IMP:UniProtKB.
GO; GO:0014033; P:neural crest cell differentiation; IMP:UniProtKB.
GO; GO:0048666; P:neuron development; IMP:UniProtKB.
GO; GO:0030182; P:neuron differentiation; IMP:UniProtKB.
GO; GO:0001764; P:neuron migration; IMP:Alzheimers_University_of_Toronto.
GO; GO:0001649; P:osteoblast differentiation; IGI:MGI.
GO; GO:0003151; P:outflow tract morphogenesis; IGI:MGI.
GO; GO:0060021; P:palate development; IGI:MGI.
GO; GO:0030220; P:platelet formation; IMP:UniProtKB.
GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; IMP:UniProtKB.
GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
GO; GO:2000987; P:positive regulation of behavioral fear response; IMP:UniProtKB.
GO; GO:0030501; P:positive regulation of bone mineralization; IMP:UniProtKB.
GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; IMP:UniProtKB.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:UniProtKB.
GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; IGI:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:2000111; P:positive regulation of macrophage apoptotic process; IMP:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:Alzheimers_University_of_Toronto.
GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:UniProtKB.
GO; GO:0090073; P:positive regulation of protein homodimerization activity; IDA:MGI.
GO; GO:2001016; P:positive regulation of skeletal muscle cell differentiation; ISO:MGI.
GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0003138; P:primary heart field specification; IMP:UniProtKB.
GO; GO:2000311; P:regulation of AMPA receptor activity; IMP:Alzheimers_University_of_Toronto.
GO; GO:0060998; P:regulation of dendritic spine development; IMP:Alzheimers_University_of_Toronto.
GO; GO:0002634; P:regulation of germinal center formation; IMP:UniProtKB.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; IMP:UniProtKB.
GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:Alzheimers_University_of_Toronto.
GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:Alzheimers_University_of_Toronto.
GO; GO:2000310; P:regulation of NMDA receptor activity; IMP:Alzheimers_University_of_Toronto.
GO; GO:0060297; P:regulation of sarcomere organization; IMP:MGI.
GO; GO:0051963; P:regulation of synapse assembly; IMP:Alzheimers_University_of_Toronto.
GO; GO:0060025; P:regulation of synaptic activity; IMP:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:Alzheimers_University_of_Toronto.
GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:Alzheimers_University_of_Toronto.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0061333; P:renal tubule morphogenesis; IMP:UniProtKB.
GO; GO:0002931; P:response to ischemia; ISS:Alzheimers_University_of_Toronto.
GO; GO:0009615; P:response to virus; IEA:Ensembl.
GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
GO; GO:0003139; P:secondary heart field specification; IMP:UniProtKB.
GO; GO:0003185; P:sinoatrial valve morphogenesis; IMP:UniProtKB.
GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
GO; GO:0051145; P:smooth muscle cell differentiation; IMP:MGI.
GO; GO:0060290; P:transdifferentiation; IEA:Ensembl.
GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; IMP:UniProtKB.
CDD; cd00265; MADS_MEF2_like; 1.
Gene3D; 3.40.1810.10; -; 1.
InterPro; IPR022102; HJURP_C.
InterPro; IPR033896; MADS_MEF2-like.
InterPro; IPR002100; TF_MADSbox.
Pfam; PF12347; HJURP_C; 1.
Pfam; PF00319; SRF-TF; 1.
PRINTS; PR00404; MADSDOMAIN.
SMART; SM00432; MADS; 1.
SUPFAM; SSF55455; SSF55455; 1.
PROSITE; PS00350; MADS_BOX_1; 1.
PROSITE; PS50066; MADS_BOX_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing; Apoptosis;
Complete proteome; Developmental protein; Differentiation;
DNA-binding; Isopeptide bond; Neurogenesis; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 474 Myocyte-specific enhancer factor 2C.
/FTId=PRO_0000199434.
DOMAIN 3 57 MADS-box. {ECO:0000255|PROSITE-
ProRule:PRU00251}.
DNA_BIND 58 86 Mef2-type. {ECO:0000255}.
REGION 271 278 Beta domain. {ECO:0000250}.
REGION 368 399 Transcription repressor. {ECO:0000250}.
COMPBIAS 4 31 Lys-rich (basic).
COMPBIAS 146 183 Ser-rich.
SITE 433 434 Cleavage. {ECO:0000305}.
MOD_RES 4 4 N6-acetyllysine.
{ECO:0000269|PubMed:18086704}.
MOD_RES 59 59 Phosphoserine; by CK2.
{ECO:0000269|PubMed:8663403}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 116 116 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q06413}.
MOD_RES 119 119 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q06413}.
MOD_RES 222 222 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 228 228 Phosphoserine.
{ECO:0000250|UniProtKB:Q06413}.
MOD_RES 234 234 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q06413}.
MOD_RES 239 239 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q06413}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 252 252 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q06413}.
MOD_RES 264 264 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q06413}.
MOD_RES 293 293 Phosphothreonine; by MAPK14.
{ECO:0000250|UniProtKB:Q06413}.
MOD_RES 300 300 Phosphothreonine; by MAPK14.
{ECO:0000250|UniProtKB:Q06413}.
MOD_RES 396 396 Phosphoserine; by CDK5.
{ECO:0000250|UniProtKB:Q06413}.
MOD_RES 420 420 Phosphoserine; by MAPK7.
{ECO:0000250|UniProtKB:Q06413}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000250|UniProtKB:Q06413}.
CROSSLNK 391 391 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 87 97 TLRKKGLNGCD -> ALNKKENKGSE (in isoform 4
and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_012501.
VAR_SEQ 103 118 ADDSVGHSPESEDKYR -> SSYALTPRTEEKYK (in
isoform 4 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_012502.
VAR_SEQ 123 134 DIDLMISRQRLC -> EFDNMIKSHKIP (in isoform
4 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_012503.
VAR_SEQ 271 278 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:8506376}.
/FTId=VSP_012504.
VAR_SEQ 368 399 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_012505.
MUTAGEN 3 3 R->T: Increased mobility in
differentiating cells. Greatly reduced
DNA binding.
{ECO:0000269|PubMed:18086704}.
MUTAGEN 4 4 K->Q: 7-fold increase in DNA binding.
{ECO:0000269|PubMed:18086704}.
MUTAGEN 4 4 K->R: Reduced acetylation by 30%. Some
loss of DNA binding and transactivation
activity. {ECO:0000269|PubMed:18086704}.
MUTAGEN 59 60 ST->CR: Reduced DNA binding activity.
MUTAGEN 59 60 ST->DD: Enhanced DNA binding activity.
MUTAGEN 59 59 S->A: Reduced DNA binding activity.
{ECO:0000269|PubMed:8663403}.
MUTAGEN 59 59 S->D: Enhanced DNA binding activity.
{ECO:0000269|PubMed:8663403}.
CONFLICT 141 141 F -> L (in Ref. 3; AAH37731).
{ECO:0000305}.
CONFLICT 211 211 S -> P (in Ref. 1). {ECO:0000305}.
CONFLICT 428 428 C -> S (in Ref. 1). {ECO:0000305}.
HELIX 22 38 {ECO:0000244|PDB:5F28}.
STRAND 42 48 {ECO:0000244|PDB:5F28}.
STRAND 54 60 {ECO:0000244|PDB:5F28}.
HELIX 62 70 {ECO:0000244|PDB:5F28}.
STRAND 77 79 {ECO:0000244|PDB:5F28}.
HELIX 81 88 {ECO:0000244|PDB:5F28}.
SEQUENCE 474 AA; 51278 MW; CEFC2DB21E89632A CRC64;
MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS TNKLFQYAST
DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCDSPD PDADDSVGHS PESEDKYRKI
NEDIDLMISR QRLCAVPPPS FEMPVTIPVS SHNSLVYSNP VSTLGNPNLL PLAHPSLQRN
SMSPGVTHRP PSAGNTGGLM GGDLTSGAGT SAGNGYGNPR NSPGLLVSPG NLNKNIQAKS
PPPMNLGMNN RKPDLRVLIP PGSKNTMPSV SEDVDLLLNQ RINNSQSAQS LATPVVSVAT
PTLPGQGMGG YPSAISTTYG TEYSLSSADL SSLSGFNTAS ALHLGSVTGW QQQHLHNMPP
SALSQLGACT STHLSQSSNL SLPSTQSLSI KSEPVSPPRD RTTTPSRYPQ HTTRHEAGRS
PVDSLSSCSS SYDGSDREDH RNEFHSPIGL TRPSPDERES PSVKRMRLSE GWAT


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